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PubMed1978

Passive transfer by cells of type II collagen-induced arthritis in rats.

To investigate the role of immunologic hypersensitivity to collagen in the causation of type II collagen-induced arthritis in rats, passive transfer experiments were performed. Wistar/Lewis rats used in these experiments were demonstrated to be histocompatible by prolonged skin graft survival and mixed lymphocyte cultures. Popliteal lymph node weight assays excluded a potential for graft-vs.-host reactivity in this strain. 9 of 32 naive rats developed arthritis after intravenous receipt of pooled spleen and lymph node cells from donors that had been injected intradermally with type II collagen emulsified in incomplete Freund's adjuvant. This passively transferred synovitis was evident clinically as well as histologically. In control cell transfer experiments involving a total of 97 recipients, transfer of arthritis was shown to require viable cells sensitized to type II collagen. These controls included 17 rats receiving cells from unimmunized donors, 20 recipients of cells from donors injected with incomplete Freund's adjuvant alone, and 24 recipients of cells from rats injected with type I collagen in adjuvant. Deliberate addition of solubilized type II collagen to unsensitized cells at the time of transfer or injection of heat-killed sensitized cells also did not cause arthritis in a total of 36 recipients. These latter two control groups indicate that disease transfer was not the result of antigen carry-over. Intravenous injection of sera from arthritic donors was incapable of passively transferring clinical or histologic synovitis in 30 recipients. Thus, these studies directly implicate immunologic sensitivity to the cartilage type of collagen in the etiology of this autoimmune disease.

Animals↗
PubMed1977

Immunological and biochemical studies of collagen type transition during in vitro chrondrogenesis of chick limb mesodermal cells.

This work describes an approach to monitor chondrogenesis of stage-24 chick limb mesodermal cells in vitro by analyzing the onset of type II collagen synthesis with carboxymethyl-cellulose chromatography, immunofluorescence, and radioimmunoassay. This procedure allowed specific and quantitative determination of chondrocytes in the presence of fibroblasts and myoblasts, both of which synthesize type I collagen. Chondrogenesis was studied in high-density cell preparations on tissue culture plastic dishes and on agar base. It was found that stage-24 limb mesenchymal cells initially synthesized only type I collagen. With the onset of chondrogenesis, a gradual transition to type II collagen synthesis was observed. In cell aggregates formed over agar, type II collagen synthesis started after 1 day in culture and reached levels of 80-90 percent of the total collagen synthesis at 6-8 days. At that time, the cells in the center of the aggregates had acquired the typical chondrocyte phenotype and stained only with type II collagen antibodies, whereas the peripheral cells had developed into a "perichondrium" and stained with type I and type II collagen antibodies. On plastic dishes plated with 5 X 10(6) cells per 35mm dish, cartilage nodules developed after 4-6 days, but the type II collagen synthesis only reached levels of 10-20 percent of the total collagen. The majority of the cells differentiated into fibroblasts and myoblasts and synthesized type I collagen. These studies demonstrate that analysis of cell specific types of collagen provides a useful method for detailing the specific events in the differentiation of mesenchymal cells in vitro.

Animals↗
PubMed1977

Synthesis of collagen by chondrocytes in suspension culture: modulation by calcium, 3':5'-cyclic AMP, and prostaglandins.

Rabbit articular chondrocytes synthesize type II collagen [3alpha(1)(II)] in vivo and type I collagen [2alpha(1)(I).alpha(2)] in monolayer cultures. In suspension culture the nature of phenotype depends on extracellular Ca(2+). The relationship of Ca(2+) and 3':5'-cyclic AMP (cAMP) in regulation of collagen synthesis has been investigated. In suspension culture, cAMP levels of chondrocytes increase by 2- to 3-fold and then reach basal values regardless of the presence or absence of extracellular Ca(2+). The cells, however, synthesize primarily type II collagen in the absence of CaCl(2) in the medium and type I collagen in medium containing 1.8 mM CaCl(2). If CaCl(2) is added when intracellular cAMP levels are low, the phenotype is type I collagen. These observations minimize the role of cAMP as a second messenger in the chondrocyte culture system. Increasing endogenous cAMP with a phosphodiesterase inhibitor or adding exogenous dibutyryl-cAMP leads the cells to synthesize type I collagen, although this effect is significantly less pronounced if the medium contains ethylene glycol bis(beta-aminoethyl ether)-N,N'-tetraacetic acid (EGTA). Increased concentrations of cAMP may mobilize the intracellular calcium pools and activate the cells to switch their phenotypic expression. Prostaglandins E(2) and F(2)alpha, thought to be involved in rheumatoid arthritis and bone resorption, have no significant effect on cAMP content of chondrocytes and alter their collagen phenotype to a small extent.

Animals↗
PubMed1979

Proteochondroitin sulfate synthesized in cartilages induced in vivo and in vitro by bone matrix gelatin.

Implanted allogeneic demineralized bone matrix gelatin induced sequential development of cartilage and bone in the recipient rat muscle tissue. Proteoglycans of the implants labeled in vivo with [35S]sulfate at different stages of development were analyzed by sucrose density gradient centrifugation. The major proteoglycan synthesized in day-5 implant, just prior to onset of chondrogenesis, was a dermatan sulfate-containing proteoglycan with relatively slow sedimentation rate. Additionally, a small amount of a faster sedimenting component could be detected. The faster sedimenting proteoglycan, in which chondroitin 4-sulfate accounted for 85% of total radioactivity, became predominant in day-10 sample when cartilage formation was maximal. By day 30, when cartilage had been replaced by newly formed bone, the synthesis of this faster sedimenting component had ceased. A similar, if not identical, proteoglycan was found to be a major one synthesized by the in vitro-induced cartilage. This proteoglycan was smaller in overall size and shorter in length of its chondroitin sulfate chains than a major proteoglycan component obtained from neonatal rat epiphyseal cartilage. Concurrent with these changes in proteoglycan type, there appeared to be a change in collagen type, since type II collagen, in addition to type I collagen, was synthesized in day-10 implant. These results indicate that the proteoglycan can be used as a molecular marker for chondrogenesis by bone matrix gelatin.

Abdominal Muscles↗
PubMed1978

Differential staining of collagens type I, II and III by Sirius Red and polarization microscopy.

Organs of fish, amphibian, reptile, bird and mammals when stained by Sirius Red and studied with polarization microscopy present different colors in regions where collagens I, II and III have been described. Collagen type I presented a yellow, orange or red color while collagen type III appeared green. Collagen type II, present in cartilage and chondrosarcoma showed a variable color according to the tissue and the species. Its color and morphology however always permitted its clear distinction from collagens type I and type III.

Animals↗
PubMed1976

Characterization of collagen and its precursors synthesized by rabbit-articular-cartilage cells in various culture systems.

Rabbit articular cartilage synthesizes type II collagen, comprised of alpha1(II) chains, in vivo or in vitro. Chondrocytes from the same tissue have the ability to produce type I chollagen with the chain composition 2alpha(I)-alpha2 or type II collagen, depending upon the culture systems in which they are maintained. Type I collagen and its precursors have been identified in the medium of monolayer cultures. Upon transfer from monolayer to suspension cultures, the cells synthesize type II collagen in the medium devoid of CaCl2 and type I collagen and its precursors in the complete medium.

Animals↗
PubMed1979

Enzyme-linked immunosorbent microassay for quantification of specific antibodies to collagen type I, II, III.

An enzyme-liked immunosorbent assay (ELISA) is described for determination of antibodies to collagen type I, II, III in serum or other body fluids. Polystyrene microplates are coated with either collagen I, II or III, and samples of body fluids being tested are incubated in the plates. Antibodies which attach specifically to the collagen are detected with anti-IgG antibody conjugated with peroxidase. Bound peroxidase is quantitatively estimated by the colour reaction produced with the substrate 5-aminosalicylic acid.

Animals↗
PubMed1978

Ultrastructural identification of type I and II collagen in the cornea of the mouse by means of enzyme labeled antibodies.

Following reaction with peroxidase-coupled IgG antibodies, collagen of both type I and type II can be demonstrated light and electron-microscopically in the cornea of the mouse by means of purified, type-specific antibodies against collagen. Both type I and type II collagen seem to be evenly distributed in the cornea, with the amount of type I exceeding that of type II.

Animals↗
PubMed1979

Changes in proline synthetic and degradative enzymes during matrix-induced cartilage and bone formation.

Proline biosynthetic and degradative enzymes are unevenly distributed in differentiated mammalian tissues. Activities of the synthetic enzymes are relatively high in collagenous tissues, whereas activities of the degradative enzymes are high in noncollagenous tissues. In order to further characterize tissue-specific proline biosynthesis and degradation, we have determined proline enzyme activities during cartilage and bone formation induced by demineralized bone matrix. We can thus follow temporal changes in enzyme activity in a single tissue as different cell types develop. Ornithine aminotransferase and pyrroline-5-carboxylate reductase have peaks of activity which correlate with maximal type II collagen synthesis by chondrocytes. Both enzymes also are active during bone formation. In contrast, proline oxidase and pyrroline-5-carboxylate dehydrogenase are present at low levels and do not change as new cell types appear. Arginase activity peaks during the first 3 days and then rapidly decreases by the time cartilage and bone formation begin. These observations further substantiate the importance of proline biosynthesis in collagenous tissues. The close correlation between ornithine aminotransferase activity and type II collagen synthesis suggests that the pathway from ornithine to proline may be especially important during formation of type II collagen.

Animals↗
PubMed1977

Collagen synthesis in normal and osteoarthritic human cartilage.

Collagen metabolism in osteoarthritic human articular cartilage was compared to that in normal cartilage and was also correlated with the degree of severity of the osteoarthritic lesion as determined by a histological-histochemical grading system. No correlation was apparent between the concentrations of DNA, hydroxyproline, and hydroxylysine and the degree of severity of the osteoarthritic lesion (except in far-advanced lesions). Similarly, there was no correlation in levels of these components in tissues from the normal vs. osteoarthritic group. The similarity of the values of the ratio hydroxylysine/hydroxyproline in osteoarthritic tissue compared with normal, and the lack of variation in these with increasing severity of the disease process argues against the possibility that osteoarthritis is associated with a major shift in the synthesis of type II collagen to type I. [3H]Proline incorporation into osteoarthritic cartilage was increased fourfold as compared to normal cartilage and varied with advancing histological-histochemical grade. Measurement of the specific activity of insolubilized hydroxyproline-containing material of the cartilage matrix, as an index of the turnover of collagen, showed a sixfold increase in osteoarthritic cartilage which also varied with grade. These data suggest that collagen synthesis in these tissues is substantially greater than in nonosteoarthritic tissues and varies directly with the severity of the disease process up to a point and then varies inversely as the lesion becomes more severe.

Cartilage, Articular↗
PubMed1979

Collagen-induced arthritis in rats. Comparison of vitreous and cartilage-derived collagens.

An oil emulsion of purified type II collagen from bovine articular cartilage when injected intradermally into rats induced an inflammatory polyarthritis in 4 of 12 animals. When similarly injected, collagen purified from bonve vitreous induced arthritis in 6 of 12 animals. Studies of humoral and cell-mediated immunity to both collagen preparations demonstrated complete cross-reactivity. It is concluded that vitreous collagen shares the arthritogenic property of cartilage-derived type II collagen and that collagen from the two sources is indistinguishable in arthritogenic and immunologic properties.

Animals↗
PubMed1976

Pepsin-solubilized collagen of human nucleus pulposus and annulus fibrosus.

Human nucleus pulposus and annulus fibrosus, obtained at autopsy from patients 7-30 years of age, were extracted with 2 M guanidine-HCl (pH 5.82) to remove proteoglycans, then stirred with pepsin in 0.5 M acetic acid, followed by three 24-h extractions with 1 M NaCl (pH 7.5) and one 24-h extraction with 2 M KSCN (potassium thiocyanate) (pH 7.2). Pepsin and NaCl solubilized an average of about 30% of nucleus pulposus collagen and 18% of annulus fibrosus collagen. KSCN extracted a further 34% of nucleus pulposus collagen and only 4% of annulus fibrosus collagen. CM-cellulose chromatography of nucleus and annulus collagen purified from the pepsin, NaCl and KSCN supernatants consistently revealed only one peak, always appearing slightly ahead of the alpha1 position for rat tail tendon type I collagen. Polyacrylamide and SDS-gel electrophoresis consistently revealed only one band with the mobility of alpha1 chains. Amino acid composition of collagen from nucleus and annulus is comparable to those of mammalian and avian cartilage type II collagen, and distinctly different from those of rat tail tendonand guinea pig skin type I collagens. Periodate oxidation of nucleus and annulus collagens showed that 81% and 67%, respectively, of the hydroxylysine residues survive treatment, compared to 71% for bovine articular cartilage collagen and 17% for guinea pig skin collagen. Total hexose analysis revealed 1.8 muM and 2.0 muM hexose per muM periodate-stable hydroxylysine in nucleus and annulus collagens, respectively. Ion exchange chromatography showed the presence of glucose and galactose in a ratio of 0.92:1 in nucleas collagen and 1.07:1 in annulus collagen. Pepsin-solubilized, NaCl-extracted collagen from nucleus and annulus formed native-type fibrils in vitro. The banding patterns of ATP-induced segment-long-spacing precipitates of nucleus and annulus collagens were identical to each other and indistinguishable from those of cartilage (type II) collagen, but distinctly different from those of rat tail tendon (type I) collagen. These data suggest that the collagen which can be extracted after limited pepsin attack of human nucleus and annulus is of the form [alpha1 (II)]3.

Adolescent↗
PubMed1975

The distribution of different molecular species of collagen in fibrous, elastic and hyaline cartilages of the pig.

The distribution of type II collagen, considered to be characteristic of cartilaginous tissues, was determined in various specialized cartilages of the mature pig. The tissues examined were: (1) fibrocartilage of the semilunar meniscus of the knee; (2) elastic cartilage of the external ear; (3) hyaline cartilage of (a) the synovial joint (b) the thyroid plate of the larynx, and (c) the nasal septum. The predominant species of collagen in each tissue, whether type I or type II, was appraised semi-quantitatively by analysis of purified collagen solubilized by pepsin and of peptide fragments produced by cyanogen bromide. Cyanogen bromide-derived peptides were characterized by column chromatography on CM-cellulose and by electrophoresis in sodium dodecyl sulphate-polyacrylamide gels. The proportion of each type of collagen was determined precisely by isolating the homologous small peptides alpha1(II)CB6 [nomenclature of Miller (1973) Clin. Orthop. 92, 260-280], by column chromatography on phosphocellulose and determining their relative proportions by amino acid analysis. Thus collagen of the fibrocartilage of the meniscus proved to be all type I; type II was not detected. In contrast, collagen of elastic cartilage of the outer ear, after rigorous exclusion of perichondrium, was type II. Similarly, type II was the only collagen detected in all the mature hyalline cartilages examined.

Amino Acids↗
PubMed1976

Cleavage of Type II and III collagens with mammalian collagenase: site of cleavage and primary structure at the NH2-terminal portion of the smaller fragment released from both collagens.

Collagenase cleavage of human Type II and III collagens has been studied using a highly purified preparation of rabbit tumor collagenase. Progress of the reactions in solution was followed by viscometry and the results indicated that under the conditions employed Type III collagen molecules were cleaved at approximately five times the rate of Type II molecules. Cleavage products of the reactions were isolated in denatured form by agarose molecular sieve chromatography. The molecular weights and amino acid compositions of the products demonstrated that Type II and III molecules had been cleaved at the characteristic three-quarter, one-quarter locus, giving rise to a large fragment derived from the NH2-terminal portion of the molecule and a smaller fragment representing the COOH-terminal region. The amino acid sequence at the NH2-terminal portion of the smaller fragment derived from Type II collagen was determined to be Ile-Ala-Gly-Gln-Arg, and the corresponding region from Type III collagen was found to have the sequence Leu-Ala Gly-Leu-Arg. These sequences for alpha1(II) and alpha1(III) chains adjacent to the site of collagenase cleavage along with previous data for alpha1(I) and alpha2 chains indicate that the minimum specific sequence required for collagenase cleavage is Gly-Ile-Ala or Gly-Leu-Ala. Inspection of the available sequence data for collagen alpha chains indicates that the latter sequences are found in at least three additional locations at which collagenase cleavage does not occur. Each of the sequences which are apparently not substrates for collagenase, however, are followed by a Gly-X-Hyp sequence. We suggest, then, that a minimum of five residues in collagen alpha chains COOH-terminal to the cleavage site comprise the substrate recognition site.

Amino Acid Sequence↗
PubMed1979

Collagen-induced arthritis in rats. Evaluation of early immunologic events.

When rats were injected intradermally with an oil emulsion of native type II collagen, they developed an inflammatory polyarthritis. The incidence and severity of arthritis increased as the amount of collagen injected was increased. Rats 4 1/2 weeks old were the most susceptible to the development of arthritis, whereas weanling and older animals were relatively resistant. There was no difference in incidence between males and females. Mononuclear cells from peripheral blood, lymph nodes, and spleen were cultured with type II collagen and responded maximally to a collagen concentration of 25 microgram/ml. The earliest detectable response was in peripheral blood mononuclear cell cultures obtained 6 to 8 days after immunization. The response of lymph node and spleen cells tended to lag behind that of peripheral blood cells at the earlier time intervals. Antibodies were detected in sera by hemagglutination at 8 days postimmunization. Quantitation of IgM and IgG antibodies by radioimmunoassay showed good correlation with hemagglutination titers and increased binding of collagen by both classes of antibody in arthritic as compared to nonarthritic animals. It is clear that the development of both humoral and cellular immunity to type II collagen is associated with the development of arthritis and may be important in the pathogenesis of this disease.

Age Factors↗
PubMed1977

Normal newborn and adult human lung collagen--analysis of types.

Previous work has shown in experimental animals that lung contains extractable collagen of types I and II and possibly III and IV. The current studies describe the types of collagen which are found in normal newborn and adult human lung. Autopsy lung specimens were dissected into tissue which was cartilage free and tissue which contained cartilage. Pleura was excluded. Extraction of distal lung which did not contain cartilage by using 1.0 M NaCl and 0.5 N acetic yielded collagen having the characteristics on acrylamide gel electrophoresis and CM-cellulose chromatography of type I collagen [alpha 1(I)] alpha2. Newborn and adult type I lung collagen are similar as compared by amino acid analysis and cyanogen bromide peptide fragment analysis. Furthermore, distal lung type I collagen is very similar, if not identical, to that found in human skin. Human bronchial cartilage collagen is similar to that found in other human cartilages. Type II collagen, [alpha 1(III)], can be extracted from human distal lung using pepsin digestion and differential salt precipitation at 1.85 M sodium chloride. This distal lung type III collagen appears identical with that found in human skin. These data support the concept that normal human lung contains collagen of types I, II, and III, identical to that found elsewhere in the body. Current techniques have not revealed a unique lung collagen. This should lead to the studies which will investigate the types and ratios of the collagens in diseased human lung.

Adult↗
PubMed1979

Production and characterization of a monoclonal antibody to chicken type I collagen.

We have shown that lymphocyte-myeloma cell hybridization can be used to produce large amounts of extremely high-titer specific antibodies against type I collagen, a macromolecule normally of low immunogenicity. In a passive hemagglutination assay the antibody had a high titer against chicken type I collagen but showed no activity against chicken type II or rat type I collagen. By using a two-step fluorescence histochemical procedure on sections of embryonic chicken tibia, strong fluorescence was observed in the perichondrium and surrounding connective tissue (known to contain type I collagen) but not over the cartilage (characterized by type II collagen). When used in conjunction with Staphylococcus aureus as a solid phase immunoadsorbant, the antibody was shown to bind to labeled collagen synthesized in vitro by embryonic chicken calvaria.

Animals↗